کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
8327246 | 1540198 | 2018 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Biochemical characterization of a highly thermostable amylosucrase from Truepera radiovictrix DSM 17093
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
![عکس صفحه اول مقاله: Biochemical characterization of a highly thermostable amylosucrase from Truepera radiovictrix DSM 17093 Biochemical characterization of a highly thermostable amylosucrase from Truepera radiovictrix DSM 17093](/preview/png/8327246.png)
چکیده انگلیسی
In this study, a novel recombinant amylosucrase from Truepera radiovictrix DSM 17093 was characterized and found to produce α-glucans from sucrose. The enzyme showed maximum total and transglucosylation activities at pHâ¯7.5 and maximum hydrolysis activity at pHâ¯5.5. The optimum temperature for total, transglucosylation, and hydrolysis activities were determined to be 45, 45, and 50â¯Â°C, respectively. When the conversion of 100â¯mM sucrose was catalyzed at 35, 45, and 55â¯Â°C for 24â¯h, TR-ASase produced α-(1,4) glucans with average DPs of 59, 45, and 37, respectively. TR-ASase displayed more than 90% of its original activity after incubation at 55â¯Â°C for 5â¯h, which was much higher than that of all other reported ASases. Melting temperature determination and homology modeling were also adopted to analyze the extreme thermostability of this enzyme, TR-ASase.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 116, September 2018, Pages 744-752
Journal: International Journal of Biological Macromolecules - Volume 116, September 2018, Pages 744-752
نویسندگان
Xingtong Zhu, Yuqing Tian, Wei Xu, Yuxiang Bai, Tao Zhang, Wanmeng Mu,